Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Meheryar N. Rivetna"'
Autor:
Jeffrey D. Hermes, Cheryl D. Schwartz, Linda S. Wicker, Barry R. Cunningham, Meheryar N. Rivetna, Elizabeth A. Nichols, Stacey J Flattery, A. Brian Jones, Richard L. Tolman
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 7:19-24
Comparison of SAR for a tetrapeptide inhibitor of MHC class II with existing information endorses a binding mode consistent with naturally loaded full length peptides.
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 5:1147-1150
Truncation of, and substitutions in, the 25 amino acid autoinhibitory element of the phosphatase calcineurin indicate that most of the segment is required for inhibition. The peptide does not, therefore, represent a convenient starting point for smal
Autor:
Francis Van Middlesworth, Susan A. Warne, Patricia Conard, Meheryar N. Rivetna, Anthony J. Conley, Emilio A. Emini, Richard L. Tolman, John Hannah, Catherine A. Dolan, Steven S. Bondy, Jon A. Rudbach, Victoria K. Rusiecki, J. Terry Ulrich, Stephen Marburg, William J. Leanza, Elizabeth E. Sugg
Publikováno v:
Vaccine. 12:445-451
A successful prophylactic human immunodeficiency virus type 1 (HIV-1) vaccine must elicit an immune response that will prevent establishment of the persistent viral infection. The only response shown to be effective in this regard is virus-neutralizi
Autor:
David W. Green, Meheryar N. Rivetna
Publikováno v:
Advances in Experimental Medicine and Biology ISBN: 9781468460148
Renin (E.C. 3.4.23.15) regulates the initial step in the generation of the potent pressor octapeptide angiotensin II by cleaving the decapeptide angiotensin I from the amino terminus of angiotensinogen (Ondetti & Cushman, 1982). In contrast to struct
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::814d7840c6da69c7d0432c859e35a5a8
https://doi.org/10.1007/978-1-4684-6012-4_49
https://doi.org/10.1007/978-1-4684-6012-4_49
Publikováno v:
Biochemistry. 28:3106-3119
In human fibrinogen Rouen, which is the origin of a bleedin disorder, a single amino acid is mutated from Gly(12) to Val(12) in the A alpha chain. In the previous paper of this series, this mutation was predicted to disrupt the structure of fibrinoge